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Activation of SAPK in Melanoma Cells
(Received for publication, September 4, 1996, and in revised form, October 28, 1996)
,
,
,
and
From the SEK-1, a dual specificity protein kinase
that serves as one of the immediate upstream activators of the
stress-activated protein kinases (SAPKs), associates specifically with
the actin-binding protein, ABP-280, in vitro and in
situ. SEK-1 binds to the carboxyl-terminal rod segment of
ABP-280, upstream of the ABP carboxyl-terminal dimerization domain.
Activation of SEK-1 in situ increases the SEK-1 activity
bound to ABP-280 without changing the amount of SEK-1 polypeptide
bound.
The influence of ABP-280 on SAPK regulation was evaluated in human
melanoma cells that lack ABP-280 expression, and in stable transformants of these cells expressing wild type ABP, or an
actin-binding but dimerization-deficient mutant ABP (ABP
Diabetes Unit and Medical Services,
Massachusetts General Hospital and Harvard Medical School, Boston,
Massachusetts 021291, ¶ Division of Experimental Medicine, Brigham
and Women's Hospital and Harvard Medical School, Boston, Massachusetts
021152, and 
National Center of Neurology and Psychiatry,
National Institute of Neuroscience, Tokyo, 187 Japan
CT109).
ABP-280-deficient cells show an activation of SAPK in response to most
stimuli that is comparable to that seen in ABP-280-replete cells;
ABP-280-deficient cells, however, fail to show the brisk tumor necrosis
factor-
(TNF-) activation of SAPK seen in ABP-replete cells and
have an 80% reduction in SAPK activation by lysophosphatidic acid. Expression of the dimerization-deficient mutant ABP-280 fails to
correct the defective SAPK response to lysophosphatidic acid, but
essentially normalizes the TNF- activation of SAPK. Thus, a lack of
ABP-280 in melanoma cells causes a defect in the regulation of SAPK
that is selective for TNF- and is attributable to the lack of
ABP-280 polypeptide itself rather than to the disordered actin
cytoskeleton that results therefrom. ABP-280 participates in TNF-
signal transduction to SAPKs, in part through the binding of SEK-1.
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